Proline residues are almost never found in short \(\alpha\) -helices; nearly all transmembrane \(\alpha\) -helices that contain proline are long ones (about \(20 \text { residues }) .\) Suggest a reason for this observation.

Short Answer

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Proline residues are less common in short alpha helices because proline's structure inhibits the formation of stabilizing hydrogen bonds, thus disrupting the helix. In long transmembrane alpha helices, however, the effect can be compensated by the rest of the structure. Furthermore, proline can induce a kink needed for transmembrane proteins to turn through the membrane's hydrophobic core.

Step by step solution

01

Structure of Proline

Proline is an amino acid. Unlike other amino acids, proline has a special structure where its side chain bonds to the amino group, creating a closed ring-like structure.
02

Proline in Alpha Helices

The alpha helix is a common protein structure stabilized by hydrogen bonds between the carbonyl group of a residue and the amino group of another residue four residues away. Because the side chain of proline is bonded to the amino group, it does not have the necessary hydrogen to participate in forming hydrogen bonds.
03

Effects on Alpha Helices

This lack of participation in hydrogen bonding makes proline a helix breaker, meaning it interrupts the regular formation of an alpha helix. This interruption would be particularly disruptive in short alpha helices, while in longer alpha helices, the disruption might be compensated by the rest of the structure.
04

Proline in Transmembrane Alpha Helices

In the case of long transmembrane alpha helices, it's suggested that the presence of proline introduces a necessary kink in the alpha helix for proteins to turn through the Hydrophobic (-CH2-) core of the membrane (a bend). This helps the protein conform to the membrane's geometry. Thus in this case, proline serves a crucial role despite its helix breaking properties.

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